Maintaining the structure of protein and peptide drugs has become one of the most important
goals of scientists in recent decades. Cold and thermal denaturation conditions …

Highlights•Liquid-liquid phase separation underlies the formation of membraneless
organelles within cells.•Theory and molecular simulations help to relate interactions at the …

Equilibrium molecular dynamics simulations, in which proteins spontaneously and
repeatedly fold and unfold, have recently been used to help elucidate the mechanistic …

▪ Abstract Heat capacity (Cp) is one of several major thermodynamic quantities commonly
measured in proteins. With more than half a dozen definitions, it is the hardest of these …

Transcription factors and other allosteric cell signaling proteins contain a disproportionate
number of domains or segments that are intrinsically disordered (ID) under native …

The process of freezing proteins is widely used in applications ranging from processing and
storage of biopharmaceuticals to cryo-EM analysis of protein complexes. The formation of an …

The interactions of biological macromolecules with water are fundamental to their structure,
dynamics and function. Historically, characterization of the location and residence times of …

Protein molecules, linear polymers of amino acids connected by peptide bonds, have
through their φ and ψ angles a freedom of rotation that endows their polypeptide chains with …

Although it is now relatively well understood how sequence defines and impacts global
protein stability in specific structural contexts, the question of how sequence modulates the …

To understand the structural basis of biology, it is necessary to understand the
transformations of macromolecules during functional cycles. These changes can involve …